dc.contributor.author | Yu, Xing | |
dc.contributor.author | Dang, Vi T | |
dc.contributor.author | Fleming, Fiona E | |
dc.contributor.author | von Itzstein, Mark | |
dc.contributor.author | Coulson, Barbara S | |
dc.contributor.author | Blanchard, Helen | |
dc.date.accessioned | 2018-01-23T01:01:21Z | |
dc.date.available | 2018-01-23T01:01:21Z | |
dc.date.issued | 2012 | |
dc.date.modified | 2013-06-17T02:42:07Z | |
dc.identifier.issn | 0022-538X | |
dc.identifier.doi | 10.1128/JVI.06975-11 | |
dc.identifier.uri | http://hdl.handle.net/10072/48644 | |
dc.description.abstract | The rotavirus spike protein domain VP8* is essential for recognition of cell-surface carbohydrate receptors, notably those incorporating N-acylneuraminic acids (members of the sialic acid family). N-acetylneuraminic acids occur naturally in both animals and humans whereas N-glycolylneuraminic acids are present only through dietary uptake in normal human tissues. The preference of animal rotaviruses towards these natural N-acylneuraminic acids has not been comprehensively established, and detailed structural information regarding the interactions of different rotaviruses with N-glycolylneuraminic acids is lacking. In this study, distinct specificities of VP8* towards N-acetyl- and N-glycolylneuraminic acids were revealed using biophysical techniques. VP8* protein from porcine rotavirus CRW-8 and bovine rotavirus NCDV showed preference for N-glycolyl- over N-acetylneuraminic acids, contrasting with monkey rotavirus RRV. Crystallographic structures of VP8* from CRW-8 and RRV with bound methyl N-glycolylneuraminide revealed the atomic details of their interactions. We examined the influence of amino acid type at position 157, which is proximal to the ligand's N-acetyl- or N-glycolyl-moiety and can mutate upon cell culture adaptation. A structure-based hypothesis derived from these results could account for rotavirus discrimination between the N-acylneuraminic acid forms. Infectivity blockade experiments demonstrated that the determined carbohydrate specificities of these VP8* directly correlate with those of the corresponding infectious virus. This includes an association between CRW-8 adaption to cell culture, decreased competition by N-glycolylneuraminic acid for CRW-8 infectivity, and a Pro157 to Ser157 mutation in VP8* that reduces binding affinity for N-glycolylneuraminic acid. | |
dc.description.peerreviewed | Yes | |
dc.description.publicationstatus | Yes | |
dc.language | English | |
dc.language.iso | eng | |
dc.publisher | American Society for Microbiology | |
dc.publisher.place | United States | |
dc.relation.ispartofstudentpublication | N | |
dc.relation.ispartofpagefrom | 13456 | |
dc.relation.ispartofpageto | 13466 | |
dc.relation.ispartofissue | 24 | |
dc.relation.ispartofjournal | Journal of Virology | |
dc.relation.ispartofvolume | 86 | |
dc.rights.retention | Y | |
dc.subject.fieldofresearch | Biomolecular Modelling and Design | |
dc.subject.fieldofresearch | Proteins and Peptides | |
dc.subject.fieldofresearch | Biological Sciences | |
dc.subject.fieldofresearch | Agricultural and Veterinary Sciences | |
dc.subject.fieldofresearch | Medical and Health Sciences | |
dc.subject.fieldofresearchcode | 030402 | |
dc.subject.fieldofresearchcode | 030406 | |
dc.subject.fieldofresearchcode | 06 | |
dc.subject.fieldofresearchcode | 07 | |
dc.subject.fieldofresearchcode | 11 | |
dc.title | Structural Basis of Rotavirus Strain Preference toward N-Acetyl- or N-Glycolylneuraminic Acid-Containing Receptors | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dc.type.code | C - Journal Articles | |
gro.faculty | Office of the Snr Dep Vice Chancellor, Institute for Glycomics | |
gro.date.issued | 2012 | |
gro.hasfulltext | No Full Text | |
gro.griffith.author | von Itzstein, Mark | |
gro.griffith.author | Coulson, Barbara | |
gro.griffith.author | Blanchard, Helen | |
gro.griffith.author | Yu, Xing | |